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Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:
Animal heme-dependent peroxidases is a family of peroxidases.Peroxidases are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, a number of animal heme peroxidases can be categorized as members of a superfamily: myeloperoxidase (MPO); eosinophil peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO); prostaglandin H synthase (PGHS); and peroxidasin.
In molecular biology, the DyP-type peroxidase family is a family of haem peroxidase enzymes. Haem peroxidases were originally divided into two superfamilies, namely, the animal peroxidases and the plant peroxidases (which are subdivided into class I, II and III), which include fungal (class II) and bacterial peroxidases. The DyP (for dye de ...
Amyloid beta, when bound to heme, has been shown to have peroxidase activity. [2] A typical group of peroxidases are the haloperoxidases. This group is able to form reactive halogen species and, as a result, natural organohalogen substances. A majority of peroxidase protein sequences can be found in the PeroxiBase database.
Heme l is the derivative of heme B which is covalently attached to the protein of lactoperoxidase, eosinophil peroxidase, and thyroid peroxidase. The addition of peroxide with the glutamyl-375 and aspartyl-225 of lactoperoxidase forms ester bonds between these amino acid residues and the heme 1- and 5-methyl groups, respectively. [19]
It was first limited to class III peroxidases (plant peroxidases) and was then expanded to include all possible haem and non-haem peroxidase protein sequences. Many researchers and bioinformaticians from the University of Geneva joined their efforts to develop the database and rapidly increase the number of peroxidase sequences.
In molecular biology, the di-haem cytochrome c peroxidase family is a group of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidizable substrate.
Horseradish peroxidase is also commonly used in techniques such as ELISA and Immunohistochemistry due to its monomeric nature and the ease with which it produces coloured products. Peroxidase, a heme-containing oxidoreductase, is a commercially important enzyme which catalyses the reductive cleavage of hydrogen peroxide by an electron donor.